dorsal/arxiv
View SchemaMultiple Folding Pathways of the SH3 domain
| Authors | J. M. Borreguero, F. Ding, S. V. Buldyrev, H. E. Stanley, N. V. Dokholyan |
|---|---|
| Categories | |
| ArXiv ID | physics/0305087 |
| URL | https://arxiv.org/abs/physics/0305087 |
| DOI | 10.1529/biophysj.104.039529 |
Abstract
Experimental observations suggest that proteins follow different pathways under different environmental conditions. We perform molecular dynamics simulations of a model of the SH3 domain over a broad range of temperatures, and identify distinct pathways in the folding transition. We determine the kinetic partition temperature --the temperature for which the SH3 domain undergoes a rapid folding transition with minimal kinetic barriers-- and observe that below this temperature the model protein may undergo a folding transition via multiple folding pathways. The folding kinetics is characterized by slow and fast pathways and the presence of only one or two intermediates. Our findings suggest the hypothesis that the SH3 domain, a protein for which only two-state folding kinetics was observed in previous experiments, may exhibit intermediates states under extreme experimental conditions, such as very low temperatures. A very recent report (Viguera et al., Proc. Natl. Acad. Sci. USA, 100:5730--5735, 2003) of an intermediate in the folding transition of the Bergerac mutant of the alpha-spectrin SH3 domain protein supports this hypothesis.
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"abstract": "Experimental observations suggest that proteins follow different pathways\nunder different environmental conditions. We perform molecular dynamics\nsimulations of a model of the SH3 domain over a broad range of temperatures,\nand identify distinct pathways in the folding transition. We determine the\nkinetic partition temperature --the temperature for which the SH3 domain\nundergoes a rapid folding transition with minimal kinetic barriers-- and\nobserve that below this temperature the model protein may undergo a folding\ntransition via multiple folding pathways. The folding kinetics is characterized\nby slow and fast pathways and the presence of only one or two intermediates.\nOur findings suggest the hypothesis that the SH3 domain, a protein for which\nonly two-state folding kinetics was observed in previous experiments, may\nexhibit intermediates states under extreme experimental conditions, such as\nvery low temperatures. A very recent report (Viguera et al., Proc. Natl. Acad.\nSci. USA, 100:5730--5735, 2003) of an intermediate in the folding transition of\nthe Bergerac mutant of the alpha-spectrin SH3 domain protein supports this\nhypothesis.",
"arxiv_id": "physics/0305087",
"authors": [
"J. M. Borreguero",
"F. Ding",
"S. V. Buldyrev",
"H. E. Stanley",
"N. V. Dokholyan"
],
"categories": [
"physics.bio-ph",
"cond-mat.soft",
"physics.chem-ph",
"q-bio"
],
"doi": "10.1529/biophysj.104.039529",
"title": "Multiple Folding Pathways of the SH3 domain",
"url": "https://arxiv.org/abs/physics/0305087"
},
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